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P14420 (PA21B_VIPAE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phospholipase A2
EC=3.1.1.4
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
Vipoxin B chain
Vipoxin non-toxic component
OrganismVipera ammodytes meridionalis (Eastern sand viper)
Taxonomic identifier73841 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Vipera

Protein attributes

Sequence length122 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

The vipoxin complex show postsynaptic neurotoxicity, while the isolated phospholipase A2 is a presynaptic neurotoxin.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

The main toxin of this snake venom is vipoxin, a complex of a toxic basic protein (B chain) having phospholipase A2 activity and a nontoxic acidic protein (A chain) functioning as its inhibitor. Without the inhibitor, the basic protein becomes unstable and within 12-14 days loses its enzymatic activity.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Miscellaneous

The supposed calcium-binding region close to Asp-48 of the basic phospholipase A2 is blocked by the side chain of Lys-60 of its inhibitor.

Sequence similarities

Belongs to the phospholipase A2 family. Group II subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 122122Phospholipase A2
PRO_0000161712

Sites

Active site471 By similarity
Active site891 By similarity
Metal binding271Calcium; via carbonyl oxygen By similarity
Metal binding291Calcium; via carbonyl oxygen By similarity
Metal binding311Calcium; via carbonyl oxygen By similarity
Metal binding481Calcium By similarity

Amino acid modifications

Disulfide bond26 ↔ 115
Disulfide bond28 ↔ 44
Disulfide bond43 ↔ 95
Disulfide bond49 ↔ 122
Disulfide bond50 ↔ 88
Disulfide bond57 ↔ 81
Disulfide bond75 ↔ 86

Secondary structure

1 ........................ 122
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14420 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 94438F9F1285FC7D

FASTA12213,828
        10         20         30         40         50         60 
NLFQFAKMIN GKLGAFSVWN YISYGCYCGW GGQGTPKDAT DRCCFVHDCC YGRVRGCNPK 

        70         80         90        100        110        120 
LAIYSYSFKK GNIVCGKNNG CLRDICECDR VAANCFHQNK NTYNKNYKFL SSSRCRQTSE 


QC

« Hide

References

[1]"Sequence homology between phospholipase and its inhibitor in snake venom. The primary structure of phospholipase A2 of vipoxin from the venom of the Bulgarian viper (Vipera ammodytes ammodytes, Serpentes)."
Mancheva I., Kleinschmidt T., Aleksiev B., Braunitzer G.
Biol. Chem. Hoppe-Seyler 368:343-352(1987) [PubMed: 3606821] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: Bulgarian.
Tissue: Venom.
[2]"Crystals of phospholipase A2 inhibitor. The non-toxic component of vipoxin from the venom of Bulgarian viper (Vipera ammodytes)."
Devedjiev Y., Atanasov B., Mancheva I., Aleksiev B.
J. Mol. Biol. 229:1147-1149(1993) [PubMed: 8445639] [Abstract]
Cited for: CRYSTALLIZATION.
Tissue: Venom.
[3]"Crystallization and preliminary X-ray analysis of vipoxin, a complex between a toxic phospholipase A2 and its natural polypeptide inhibitor."
Betzel C., Visanji M., Wilson K.S., Genov N., Mancheva I., Aleksiev B., Singh T.P.
J. Mol. Biol. 231:498-500(1993) [PubMed: 8510159] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Tissue: Venom.
[4]"Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution."
Perbandt M., Wilson J.C., Eschenburg S., Mancheva I., Aleksiev B., Genov N., Willingmann P., Weber W., Singh T.P., Betzel C.
FEBS Lett. 412:573-577(1997) [PubMed: 9276469] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
[5]"Structure of the neurotoxic complex vipoxin at 1.4 A resolution."
Banumathi S., Rajashankar K.R., Notzel C., Aleksiev B., Singh T.P., Genov N., Betzel C.
Acta Crystallogr. D 57:1552-1559(2001) [PubMed: 11679719] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRA29290.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOKX-ray2.00B1-118[»]
1JLTX-ray1.40B1-122[»]
1RGBX-ray3.30A/B/K/L1-122[»]
ProteinModelPortalP14420.
SMRP14420. Positions 1-122.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-220273.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008137.

Family and domain databases

InterProIPR016090. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR001211. PLipase_A2_euk.
[Graphical view]
Gene3DG3DSA:1.20.90.10. Phospholipase_A2. 1 hit.
PANTHERPTHR11716. Phospholipase_A2. 1 hit.
PfamPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSPR00389. PHPHLIPASEA2.
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMSSF48619. PhospholipaseA2. 1 hit.
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePA21B_VIPAE
AccessionPrimary (citable) accession number: P14420
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 16, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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